Cargando…

Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy

α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same bindi...

Descripción completa

Detalles Bibliográficos
Autores principales: Li, Yifang, Tan, Hongxia, Zhou, Hongyuan, Guo, Ting, Zhou, Ying, Zhang, Yuhao, Liu, Xiaozhu, Ma, Liang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9501389/
https://www.ncbi.nlm.nih.gov/pubmed/36136542
http://dx.doi.org/10.3390/toxins14090604
_version_ 1784795462602063872
author Li, Yifang
Tan, Hongxia
Zhou, Hongyuan
Guo, Ting
Zhou, Ying
Zhang, Yuhao
Liu, Xiaozhu
Ma, Liang
author_facet Li, Yifang
Tan, Hongxia
Zhou, Hongyuan
Guo, Ting
Zhou, Ying
Zhang, Yuhao
Liu, Xiaozhu
Ma, Liang
author_sort Li, Yifang
collection PubMed
description α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 10(5) M(−1), which is higher than that of α-ZOL (3.98 × 10(4) M(−1)). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure.
format Online
Article
Text
id pubmed-9501389
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-95013892022-09-24 Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy Li, Yifang Tan, Hongxia Zhou, Hongyuan Guo, Ting Zhou, Ying Zhang, Yuhao Liu, Xiaozhu Ma, Liang Toxins (Basel) Article α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 10(5) M(−1), which is higher than that of α-ZOL (3.98 × 10(4) M(−1)). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure. MDPI 2022-08-31 /pmc/articles/PMC9501389/ /pubmed/36136542 http://dx.doi.org/10.3390/toxins14090604 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Yifang
Tan, Hongxia
Zhou, Hongyuan
Guo, Ting
Zhou, Ying
Zhang, Yuhao
Liu, Xiaozhu
Ma, Liang
Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title_full Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title_fullStr Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title_full_unstemmed Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title_short Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
title_sort study of competitive displacement of curcumin on α-zearalenol binding to human serum albumin complex using fluorescence spectroscopy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9501389/
https://www.ncbi.nlm.nih.gov/pubmed/36136542
http://dx.doi.org/10.3390/toxins14090604
work_keys_str_mv AT liyifang studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT tanhongxia studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT zhouhongyuan studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT guoting studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT zhouying studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT zhangyuhao studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT liuxiaozhu studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy
AT maliang studyofcompetitivedisplacementofcurcuminonazearalenolbindingtohumanserumalbumincomplexusingfluorescencespectroscopy